IndraLab

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USP1 deubiquitinates MAX. 5 / 5
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"Overexpression of USP1 prolonged the half-life of MAX/MYC protein and decreased the ubiquitination of MAX/MYC protein."
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"Our study showed that inhibition of USP1 by shRNA or pimozide treatment significantly increased the ubiquitination of MAX/MYC and reduced the protein levels of MAX/MYC in rituximab/chemotherapy resistant DLBCL cells, which led to the decrease of MYC target genes and the growth inhibition of lymphoma cells in the cell or patient-derived DLBCL mouse model."
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"USP1 deubiquitinates MAX, which is an important MYC-binding protein and promotes MYC gene transcription."
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"Furthermore, USP1 knockdown enhanced ubiquitylation of the MAX but not MAX mutant (Supplementary Fig. S4c)."
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"Together, these data demonstrated that USP1 deubiquitinated and stabilized MAX and MYC proteins in rituximab/chemotherapy resistant DLBCL cells."
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